Evidence map›Paper›PMID 40347946›Full record

ArticleCell reports methods2025

Site-specific quantification of the in vivo UFMylome reveals myosin modification in ALS.

Ronnie Blazev, Barry M Zee, Hayley Peckham, Yaan-Kit Ng, Christopher T A Lewis, Chengxin Zhang, James W McNamara, Craig A Goodman, Paul Gregorevic, Julien Ochala and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Ronnie BlazevDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia.
Barry M ZeeCell Signaling Technology, Danvers, MA 01923, USA.
Hayley PeckhamCell Signaling Technology, Danvers, MA 01923, USA.
Yaan-Kit NgDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia.
Christopher T A LewisDepartment of Biomedical Sciences, University of Copenhagen, 1165 Copenhagen, Denmark; Novo Nordisk A/S, Research and Early Development, 2760 Måløv, Denmark.
Chengxin ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48104, USA.
James W McNamaraDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia; Murdoch Children's Research Institute and Melbourne Centre for Cardiovascular Genomics and Regenerative Medicine, The Royal Children's Hospital, Parkville, VIC 3052, Australia; Melbourne Centre for Cardiovascular Genomics and Regenerative Medicine, The Royal Children's Hospital, Melbourne, VIC 3052, Australia; Novo Nordisk Foundation Center for Stem Cell Medicine, Murdoch Children's Research Institute, Melbourne, VIC 3052, Australia.
Craig A GoodmanDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia.
Paul GregorevicDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia; Department of Neurology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Julien OchalaDepartment of Biomedical Sciences, University of Copenhagen, 1165 Copenhagen, Denmark.
Frederik J SteynDepartment of Neurology, Royal Brisbane and Women's Hospital, Brisbane, QLD 4029, Australia; School of Biomedical Sciences, The University of Queensland, Brisbane, QLD 4072, Australia.
Shyuan T NgoDepartment of Neurology, University of Washington School of Medicine, Seattle, WA 98195, USA; Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia; Centre for Clinical Research, The University of Queensland, Brisbane, QLD 4029, Australia.
Matthew P StokesCell Signaling Technology, Danvers, MA 01923, USA.
Benjamin L ParkerDepartment of Anatomy and Physiology, The University of Melbourne, Parkville, VIC 3010, Australia; Centre for Muscle Research, The University of Melbourne, Parkville, VIC 3010, Australia. Electronic address: ben.parker@unimelb.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UFMylation is a ubiquitin-like protein modification of Ubiquitin Fold Modifier 1 (UFM1) applied to substrate proteins and regulates several cellular processes such as protein quality control. Here, we describe the development of an antibody-based enrichment approach to immunoprecipitate remnant UFMylated peptides and identification by mass spectrometry. We used this approach to identify >200 UFMylation sites from various mouse tissues, revealing extensive modification in skeletal muscle. In vivo knockdown of the E2 ligase, UFC1, followed by enrichment and analysis of remnant UFMylated peptides quantified concomitant down-regulation and validation of a subset of modification sites, particularly myosin UFMylation. Furthermore, we show that UFMylation is increased in skeletal muscle biopsies from people living with amyotrophic lateral sclerosis (plwALS). Quantification of UFMylation sites in these biopsies with multiplexed isotopic labeling reveal prominent increases in myosin UFMylation. Our data suggest that in vivo UFMylation is more complex than previously thought.

Indexed as

Amyotrophic Lateral SclerosisMyosinsUbiquitinsAnimalsHumansMass SpectrometryMiceMuscle, SkeletalProtein Processing, Post-TranslationalUbiquitinationMyosinsUbiquitinsCP: cell biologyUbiquitin Fold Modifier 1ubiquitin-like modificationUFM1UFMylation

Identifiers

PMID40347946
PMCPMC12146631

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.